Pub Date : 2024-10-01DOI: 10.1016/j.foostr.2024.100394
Muhammad Faiz Bin Muhd Faizal Abdullah Tan , Oni Yuliarti , Adeline Ik Chian Wong , Jerome Jie Long Wong
The effects of pectin addition with low degree esterification on wheat noodles’ physicochemical properties such as texture and in vitro starch digestibility were investigated. Wheat flour was incorporated with low methoxyl pectin (LMP) at five levels: 0 %, 0.5 %, 1 %, 2 % and 4 % w/w in calcium fortified wheat noodles. As LMP incorporation increased to 4 % w/w, noodle water absorption declined, due to formation of LMP gels. Noodles textural results revealed an increase in hardness, gumminess, cohesiveness and adhesiveness due to the increase in noodle thickness which corresponded well with noodle microstructure results. Rheological measurements showed an increase in wheat noodle viscoelastic properties as a result of addition of LMP. Similar results are also shown on the pasting profiles, where peak, trough and final viscosity were raised with the incorporation of LMP. Overall findings showed the incorporation of LMP was able to lower the in vitro starch digestibility, where addition of 2 % w/w resulted in the highest reduction. These results successfully indicated the LMP’s potential to be used as an ingredient in carbohydrate dense foods such as wheat noodle to retard starch digestion.
{"title":"Structural and in vitro starch digestion of wheat flour noodles by calcium mediated gelation of low methoxyl pectin","authors":"Muhammad Faiz Bin Muhd Faizal Abdullah Tan , Oni Yuliarti , Adeline Ik Chian Wong , Jerome Jie Long Wong","doi":"10.1016/j.foostr.2024.100394","DOIUrl":"10.1016/j.foostr.2024.100394","url":null,"abstract":"<div><div>The effects of pectin addition with low degree esterification on wheat noodles’ physicochemical properties such as texture and <em>in vitro</em> starch digestibility were investigated. Wheat flour was incorporated with low methoxyl pectin (LMP) at five levels: 0 %, 0.5 %, 1 %, 2 % and 4 % w/w in calcium fortified wheat noodles. As LMP incorporation increased to 4 % w/w, noodle water absorption declined, due to formation of LMP gels. Noodles textural results revealed an increase in hardness, gumminess, cohesiveness and adhesiveness due to the increase in noodle thickness which corresponded well with noodle microstructure results. Rheological measurements showed an increase in wheat noodle viscoelastic properties as a result of addition of LMP. Similar results are also shown on the pasting profiles, where peak, trough and final viscosity were raised with the incorporation of LMP. Overall findings showed the incorporation of LMP was able to lower the <em>in vitro</em> starch digestibility, where addition of 2 % w/w resulted in the highest reduction. These results successfully indicated the LMP’s potential to be used as an ingredient in carbohydrate dense foods such as wheat noodle to retard starch digestion.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100394"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142420494","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-01DOI: 10.1016/j.foostr.2024.100397
N.I. Salgarella , A. Bonciolini , V. Glicerina , M. Greco Miani , H.D. Tatar , V. Cardenia
Durum wheat oil (WO) is a by-product obtained during wheat milling process characterized by higher amount of bioactive compounds. In recent years, oleogelification, a novel technique to structure oils was developed to replace saturated and trans fats. The aim of this study was to evaluate the performances of WO to obtain stable oleogels using two natural waxes (beeswax BW and carnauba wax CW) at different ratio (4, 7 and 8 %, w/w) respect to sunflower oil (SO) used as control. Oleogels were analyzed for fundamental rheological properties, microstructure and oil loss. Results showed as a concentration below 7 %, weak networks were observed for all samples because the predominance of viscous moduli (G’’) over elastic ones (G’) and high oil loss. Nevertheless at 8 % of waxes, stability in terms of all analyzed parameters was highlighted for all samples (WO_BW showed the lowest). Moreover, WO samples with 7 % and 8 % of CW displayed very high stability in terms of all considered parameters, also at high temperatures, showing strong networks and reaching the optimum solid-like gel without significant differences respect to SO one. Obtained results highlighted the WO ability to be employed, as alternative to SO to develop oleogels with optimal performances and stability.
硬质小麦油（WO）是小麦碾磨过程中产生的一种副产品，其特点是含有较多的生物活性化合物。近年来，人们开发了油凝胶化这一新型油脂结构技术，以取代饱和脂肪和反式脂肪。本研究旨在评估使用两种天然蜡（蜂蜡 BW 和棕榈蜡 CW）以不同比例（4%、7% 和 8%，w/w）获得稳定油凝胶的 WO 性能，而葵花籽油（SO）则作为对照。对油凝胶的基本流变特性、微观结构和油流失进行了分析。结果表明，当浓度低于 7% 时，所有样品的网络都很薄弱，因为粘模量（G''）比弹性模量（G'）大，而且油分损失也很高。然而，当蜡含量达到 8% 时，所有样品在所有分析参数方面的稳定性都很突出（WO_BW 的稳定性最低）。此外，CW 含量为 7% 和 8% 的 WO 样品在所有考虑参数方面都显示出极高的稳定性，在高温下也是如此，显示出很强的网络性，达到了最佳的固态凝胶状态，与 SO 样品没有明显差异。所获得的结果凸显了使用 WO 替代 SO 开发具有最佳性能和稳定性的油凝胶的能力。
{"title":"Durum wheat oil oleogels: A study on rheological, thermal, and microstructural properties","authors":"N.I. Salgarella , A. Bonciolini , V. Glicerina , M. Greco Miani , H.D. Tatar , V. Cardenia","doi":"10.1016/j.foostr.2024.100397","DOIUrl":"10.1016/j.foostr.2024.100397","url":null,"abstract":"<div><div>Durum wheat oil (WO) is a by-product obtained during wheat milling process characterized by higher amount of bioactive compounds. In recent years, oleogelification, a novel technique to structure oils was developed to replace saturated and <em>trans</em> fats. The aim of this study was to evaluate the performances of WO to obtain stable oleogels using two natural waxes (beeswax BW and carnauba wax CW) at different ratio (4, 7 and 8 %, <em>w/w</em>) respect to sunflower oil (SO) used as control. Oleogels were analyzed for fundamental rheological properties, microstructure and oil loss. Results showed as a concentration below 7 %, weak networks were observed for all samples because the predominance of viscous moduli (G’’) over elastic ones (G’) and high oil loss. Nevertheless at 8 % of waxes, stability in terms of all analyzed parameters was highlighted for all samples (WO_BW showed the lowest). Moreover, WO samples with 7 % and 8 % of CW displayed very high stability in terms of all considered parameters, also at high temperatures, showing strong networks and reaching the optimum solid-like gel without significant differences respect to SO one. Obtained results highlighted the WO ability to be employed, as alternative to SO to develop oleogels with optimal performances and stability.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100397"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142526539","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-01DOI: 10.1016/j.foostr.2024.100402
Jiayi Li , Nan Xiao , Shanguang Guo , Minmin Ai
To improve the freeze-thaw stability of the emulsion, a Pickering emulsion stabilized by grafted protein was prepared and characterized through blending with hyaluronic acid (HA) and trehalose (TH). The results indicated that HA crosslinked with proteins to form a surface coating on the droplets. TH prevented aggregation by imparting spatial repulsion, when combined with HA, resulted in a significant reduction in emulsion particle size from 35.95 μm to 22.99 μm. The emulsion showed well stability against droplet flocculation after freeze-thaw cycles. Microstructural observation revealed that the cross-linking of HA and TH inhibited the ice crystal damage. In-vitro digestive characterization indicated that HA and TH prevented digestive enzymes from destroying the droplet structure, realising efficient delivery of curcumin. Among them, the bioaccessibility and stability of curcumin were improved by 8.19 % and 15.25 %. Moreover, 1HNMR analysis demonstrated that the stabilization of HA and TH at the oil-water interface improved the antioxidant properties of the emulsion.
{"title":"Grafted egg white protein-stabilized Pickering emulsions mediated by saccharide: Enhancing freeze-thaw stability and delayed release of curcumin from digestion","authors":"Jiayi Li , Nan Xiao , Shanguang Guo , Minmin Ai","doi":"10.1016/j.foostr.2024.100402","DOIUrl":"10.1016/j.foostr.2024.100402","url":null,"abstract":"<div><div>To improve the freeze-thaw stability of the emulsion, a Pickering emulsion stabilized by grafted protein was prepared and characterized through blending with hyaluronic acid (HA) and trehalose (TH). The results indicated that HA crosslinked with proteins to form a surface coating on the droplets. TH prevented aggregation by imparting spatial repulsion, when combined with HA, resulted in a significant reduction in emulsion particle size from 35.95 μm to 22.99 μm. The emulsion showed well stability against droplet flocculation after freeze-thaw cycles. Microstructural observation revealed that the cross-linking of HA and TH inhibited the ice crystal damage. In-vitro digestive characterization indicated that HA and TH prevented digestive enzymes from destroying the droplet structure, realising efficient delivery of curcumin. Among them, the bioaccessibility and stability of curcumin were improved by 8.19 % and 15.25 %. Moreover, <sup>1</sup>HNMR analysis demonstrated that the stabilization of HA and TH at the oil-water interface improved the antioxidant properties of the emulsion.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100402"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697931","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Several studies have been performed to improve structural, nutritional and functional properties of proteins through protein-phenolic interactions. In this study, changes in the structure of chickpea protein following interaction with spent coffee phenolics were analyzed. Varying phenolic concentrations (0, 0.5, 1.0, and 1.5) and pH values (7.0 and 9.0) were examined to investigate the effect of different interaction conditions. The results indicated that spent coffee phenolics induced the secondary and tertiary structure of chickpea protein, and this change was affected by the phenolic concentration. The interaction with phenolic compounds resulted in a blue shift in the FTIR spectra in Amide A at both pH values. Chickpea protein isolate (CPI) reacted with phenolic compounds via C-N and N-H bonds and hydrogen bonds were built up between protein-phenolic complexes. Thermodynamic parameter calculations indicated that hydrogen bonding and van der Waals forces were the primary types of interactions between CPI and phenolic extract at both pH conditions (7.0 and 9.0). Besides, irregularity of shapes was observed in morphological analysis after protein-phenolic interaction. In addition to proven structural changes, this study has laid the basis for future studies investigating the effect of phenolics on the functional and nutritional properties of chickpea proteins.
{"title":"Binding kinetics and structural analysis of chickpea protein interactions with spent coffee phenolics under varying pH and concentrations","authors":"Beyza Saricaoglu , Hilal Yılmaz , Busra Gultekin Subasi , Mohammad Amin Mohammadifar , Esra Capanoglu","doi":"10.1016/j.foostr.2024.100401","DOIUrl":"10.1016/j.foostr.2024.100401","url":null,"abstract":"<div><div>Several studies have been performed to improve structural, nutritional and functional properties of proteins through protein-phenolic interactions. In this study, changes in the structure of chickpea protein following interaction with spent coffee phenolics were analyzed. Varying phenolic concentrations (0, 0.5, 1.0, and 1.5) and pH values (7.0 and 9.0) were examined to investigate the effect of different interaction conditions. The results indicated that spent coffee phenolics induced the secondary and tertiary structure of chickpea protein, and this change was affected by the phenolic concentration. The interaction with phenolic compounds resulted in a blue shift in the FTIR spectra in Amide A at both pH values. Chickpea protein isolate (CPI) reacted with phenolic compounds via C-N and N-H bonds and hydrogen bonds were built up between protein-phenolic complexes. Thermodynamic parameter calculations indicated that hydrogen bonding and van der Waals forces were the primary types of interactions between CPI and phenolic extract at both pH conditions (7.0 and 9.0). Besides, irregularity of shapes was observed in morphological analysis after protein-phenolic interaction. In addition to proven structural changes, this study has laid the basis for future studies investigating the effect of phenolics on the functional and nutritional properties of chickpea proteins.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100401"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697932","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-01DOI: 10.1016/j.foostr.2024.100398
Jarupat Luecha , Jens Saalbrink , José C. Bonilla , Nesli Sozer
Pea protein ingredients play key role in formulations of plant-based foods. However, functional properties of pea ingredients are inconsistent depending on extraction process. Protein aggregation occurs simultaneously during protein extraction, thus examining the protein aggregated states as induced by processing is essential for better process design. This study investigated the influence of process-induced protein aggregated states on structure formation upon heating of pea protein ingredients. Combining rheological, spectroscopic, and microscopic techniques, the mechanisms underlining heat-induced structure formation have been unveiled from microscopic to macroscopic scales. The salt-extracted isolate (PPI*) where protein aggregation was minimized, developed mesh-like structure through intermolecular protein-protein interaction upon gelling similar to commercial protein concentrate (PPC). In turn, commercial isolate (PPI) as appeared as microscopic particles, formed gel through accumulation of protein particles with no structure development. The aggregated states of PPI* and PPI seemed to dictate vicilin and legumin purification by means of anion exchange chromatography. Purification process promoted intermolecular protein aggregate structures. However, these purified fractions regardless of parent isolates showed similar structure development as PPC and PPI* during gelling. Monitoring protein aggregation during extraction process can be a key to limit functional property variation in pea protein ingredients.
豌豆蛋白成分在植物性食品配方中发挥着关键作用。然而，豌豆成分的功能特性因提取工艺的不同而不尽相同。蛋白质提取过程中会同时出现蛋白质聚集现象，因此研究加工过程诱导的蛋白质聚集状态对于更好地设计加工过程至关重要。本研究调查了豌豆蛋白成分加热后，加工过程诱导的蛋白质聚集状态对结构形成的影响。结合流变学、光谱学和显微镜技术，从微观到宏观揭示了热诱导结构形成的基本机制。盐提取分离物（PPI*）的蛋白质聚集程度最小，在胶凝过程中通过分子间蛋白质-蛋白质相互作用形成网状结构，与商业浓缩蛋白（PPC）类似。反之，商业分离物（PPI）则以微小颗粒的形式出现，通过蛋白质颗粒的聚集形成凝胶，结构没有形成。PPI* 和 PPI 的聚集状态似乎决定了用阴离子交换色谱法纯化维卡林和豆蛋白。纯化过程促进了分子间蛋白质聚集结构的形成。然而，这些纯化馏分无论母体分离物如何，在胶凝过程中都表现出与 PPC 和 PPI* 相似的结构发展。在提取过程中监控蛋白质聚集是限制豌豆蛋白成分功能特性变化的关键。
{"title":"Process-induced protein aggregates influenced pea globulins’ structure formation upon heating","authors":"Jarupat Luecha , Jens Saalbrink , José C. Bonilla , Nesli Sozer","doi":"10.1016/j.foostr.2024.100398","DOIUrl":"10.1016/j.foostr.2024.100398","url":null,"abstract":"<div><div>Pea protein ingredients play key role in formulations of plant-based foods. However, functional properties of pea ingredients are inconsistent depending on extraction process. Protein aggregation occurs simultaneously during protein extraction, thus examining the protein aggregated states as induced by processing is essential for better process design. This study investigated the influence of process-induced protein aggregated states on structure formation upon heating of pea protein ingredients. Combining rheological, spectroscopic, and microscopic techniques, the mechanisms underlining heat-induced structure formation have been unveiled from microscopic to macroscopic scales. The salt-extracted isolate (PPI*) where protein aggregation was minimized, developed mesh-like structure through intermolecular protein-protein interaction upon gelling similar to commercial protein concentrate (PPC). In turn, commercial isolate (PPI) as appeared as microscopic particles, formed gel through accumulation of protein particles with no structure development. The aggregated states of PPI* and PPI seemed to dictate vicilin and legumin purification by means of anion exchange chromatography. Purification process promoted intermolecular protein aggregate structures. However, these purified fractions regardless of parent isolates showed similar structure development as PPC and PPI* during gelling. Monitoring protein aggregation during extraction process can be a key to limit functional property variation in pea protein ingredients.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100398"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142555584","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-01DOI: 10.1016/j.foostr.2024.100400
Yurou Chen, Mengyue Zhang, Yuhan Lan, Xibo Wang
This study aims to enhance the flexibility of soy protein isolate (SPI) to improve its functional properties, focusing on the investigated the effects of ferulic acid (FA) on the structure, interfacial behaviour and emulsification performance of SPI. Our study showed that FA induces SPI structures to depolymerization and unfolding primarily through hydrogen bonding and hydrophobic interactions, thereby increasing the flexible structures (random coils and β-turns) of protein. These changes enhanced the interfacial functional properties of SPI, with 150 μmol/g of FA-modified SPI exhibiting the best molecular flexibility, and its emulsification and emulsification stability were improved by 21.26 % and 39.86 %, respectively, compared to unmodified SPI. In addition, non-covalently modified FA significantly improved emulsions stability. Emulsions stabilized by SPI-FA150 complexes exhibited better storage, heat, and freeze-thaw stability than SPI, with a significant reduction in oxidation products. This relationship between flexibility and function reveals the importance of structural modification in enhancing protein functionality. These discoveries shed new light on flexible protein processing technologies and the application of FA in protein functional modification.
本研究旨在提高大豆分离蛋白（SPI）的柔韧性，从而改善其功能特性，重点研究阿魏酸（FA）对 SPI 结构、界面行为和乳化性能的影响。我们的研究表明，阿魏酸主要通过氢键和疏水作用诱导 SPI 结构解聚和展开，从而增加了蛋白质的柔性结构（无规线圈和 β-匝）。这些变化增强了 SPI 的界面功能特性，其中 150 μmol/g 的 FA 改性 SPI 表现出最佳的分子柔性，与未改性 SPI 相比，其乳化性和乳化稳定性分别提高了 21.26 % 和 39.86 %。此外，非共价改性的 FA 也显著提高了乳液的稳定性。与 SPI 相比，经 SPI-FA150 复合物稳定的乳液具有更好的储存稳定性、热稳定性和冻融稳定性，氧化产物也明显减少。柔性与功能之间的这种关系揭示了结构修饰在增强蛋白质功能方面的重要性。这些发现为柔性蛋白质加工技术和 FA 在蛋白质功能修饰中的应用提供了新的思路。
{"title":"Enhancing soy protein isolate flexibility through non-covalent ferulic acid modification: Implications for interfacial characteristics and protein-based emulsion performance","authors":"Yurou Chen, Mengyue Zhang, Yuhan Lan, Xibo Wang","doi":"10.1016/j.foostr.2024.100400","DOIUrl":"10.1016/j.foostr.2024.100400","url":null,"abstract":"<div><div>This study aims to enhance the flexibility of soy protein isolate (SPI) to improve its functional properties, focusing on the investigated the effects of ferulic acid (FA) on the structure, interfacial behaviour and emulsification performance of SPI. Our study showed that FA induces SPI structures to depolymerization and unfolding primarily through hydrogen bonding and hydrophobic interactions, thereby increasing the flexible structures (random coils and β-turns) of protein. These changes enhanced the interfacial functional properties of SPI, with 150 μmol/g of FA-modified SPI exhibiting the best molecular flexibility, and its emulsification and emulsification stability were improved by 21.26 % and 39.86 %, respectively, compared to unmodified SPI. In addition, non-covalently modified FA significantly improved emulsions stability. Emulsions stabilized by SPI-FA<sub>150</sub> complexes exhibited better storage, heat, and freeze-thaw stability than SPI, with a significant reduction in oxidation products. This relationship between flexibility and function reveals the importance of structural modification in enhancing protein functionality. These discoveries shed new light on flexible protein processing technologies and the application of FA in protein functional modification.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100400"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142663033","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The present study aimed at utilization of aqueous extract and fiber-rich extraction residue of defatted date seed powder (DDSP) as functional ingredient for improving the quality attributes of biscuit dough. Previously optimized microwave-assisted extraction (MAE) was used to recover the bioactive compounds from small, medium and large sized DDSP particles. Extracts and 2.5 %, 5 % and 7.5 % substitution levels of fiber-rich residue were incorporated in dough formulations, before rheological, physical and bioactive properties of dough were investigated. Smallest particles at 7.5 % substitution level resulted in the highest storage (G′) and loss moduli (G″) and lowest creep strain showing the highest resistance to deformation in the dough. Hardness increased with decreasing particle size and increasing substitution level of extraction residue. Highest substitution level with smallest particle size resulted in the darkest dough. Highest total phenolic content (TPC) of 0.60 mg GAE/g was found in the dough with 7.5 % substitution level by medium sized particles. The highest DPPH radical scavenging activity and Ferric reducing antioxidant power (FRAP) values were 2.00 mmol TE/g and 0.34 mmol TE/g, respectively, for small sized particles and 7.5 % substitution level of extraction residue. Substitution of DDSP fiber-rich extraction residue altered the structural arrangement of gluten in the dough.
{"title":"Changes in the rheological, textural, microstructural and in vitro antioxidant properties of biscuit dough by incorporation of the extract and fiber-rich residue obtained through green extraction of defatted date seeds","authors":"Meththa Ranasinghe , Constantinos Stathopoulos , Balan Sundarakani , Sajid Maqsood","doi":"10.1016/j.foostr.2024.100395","DOIUrl":"10.1016/j.foostr.2024.100395","url":null,"abstract":"<div><div>The present study aimed at utilization of aqueous extract and fiber-rich extraction residue of defatted date seed powder (DDSP) as functional ingredient for improving the quality attributes of biscuit dough. Previously optimized microwave-assisted extraction (MAE) was used to recover the bioactive compounds from small, medium and large sized DDSP particles. Extracts and 2.5 %, 5 % and 7.5 % substitution levels of fiber-rich residue were incorporated in dough formulations, before rheological, physical and bioactive properties of dough were investigated. Smallest particles at 7.5 % substitution level resulted in the highest storage (G′) and loss moduli (G″) and lowest creep strain showing the highest resistance to deformation in the dough. Hardness increased with decreasing particle size and increasing substitution level of extraction residue. Highest substitution level with smallest particle size resulted in the darkest dough. Highest total phenolic content (TPC) of 0.60 mg GAE/g was found in the dough with 7.5 % substitution level by medium sized particles. The highest DPPH radical scavenging activity and Ferric reducing antioxidant power (FRAP) values were 2.00 mmol TE/g and 0.34 mmol TE/g, respectively, for small sized particles and 7.5 % substitution level of extraction residue. Substitution of DDSP fiber-rich extraction residue altered the structural arrangement of gluten in the dough.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100395"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142420495","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-01DOI: 10.1016/j.foostr.2024.100399
Sajed Amjadi , Hadi Almasi , Hamed Hamishehkar , Morteza Kashaninejad , Ali Ehsani , Shirin Jalili
The objective of this study was to investigate the co-loading of vitamin D3 (VitD3) and Spirulina platensis protein hydrolysates (SPH) within coated nanoliposomes (NLPs) by sodium caseinate, with the intention of developing a novel nutritional supplement. The coated NLPs exhibited particle size, PDI, and zeta potential values of 185.30 ± 29.62 nm, 0.22±0.04, and +18.70 ± 3.44 mV, respectively. Moreover, the encapsulation efficiencies of the coated NLPs for VitD3 and SPH were 83.24 ± 4.22 % and 89.41 ± 4.36 %, respectively. The improving effect of the surface coating by sodium caseinate on the stability and function of the NLPs was exhibited through analysis of chemical structure, thermal stability, and crystalline structure. The transmission electron microscopy pictures of the developed NLPs revealed a spherical morphology with a thin layer around the vesicle. The loaded VitD3 and SPH in the coated NLPs showed controlled release profiles during incubation in the simulated gastrointestinal condition. Moreover, the VitD3/SPH co-loaded NLPs and their coated form had no considerable cell toxicity. To conclude, the developed nanosystem demonstrated the suitable characteristics of a nanocarrier for reaping the nutritional benefits of VitD3 and SPH.
{"title":"Development of vitamin D3 and Spirulina platensis protein hydrolysates co-loaded nanoliposomes and coated by sodium caseinate","authors":"Sajed Amjadi , Hadi Almasi , Hamed Hamishehkar , Morteza Kashaninejad , Ali Ehsani , Shirin Jalili","doi":"10.1016/j.foostr.2024.100399","DOIUrl":"10.1016/j.foostr.2024.100399","url":null,"abstract":"<div><div>The objective of this study was to investigate the co-loading of vitamin D<sub>3</sub> (VitD<sub>3</sub>) and <em>Spirulina platensis</em> protein hydrolysates (SPH) within coated nanoliposomes (NLPs) by sodium caseinate, with the intention of developing a novel nutritional supplement. The coated NLPs exhibited particle size, PDI, and zeta potential values of 185.30 ± 29.62 nm, 0.22±0.04, and +18.70 ± 3.44 mV, respectively. Moreover, the encapsulation efficiencies of the coated NLPs for VitD<sub>3</sub> and SPH were 83.24 ± 4.22 % and 89.41 ± 4.36 %, respectively. The improving effect of the surface coating by sodium caseinate on the stability and function of the NLPs was exhibited through analysis of chemical structure, thermal stability, and crystalline structure. The transmission electron microscopy pictures of the developed NLPs revealed a spherical morphology with a thin layer around the vesicle. The loaded VitD<sub>3</sub> and SPH in the coated NLPs showed controlled release profiles during incubation in the simulated gastrointestinal condition. Moreover, the VitD<sub>3</sub>/SPH co-loaded NLPs and their coated form had no considerable cell toxicity. To conclude, the developed nanosystem demonstrated the suitable characteristics of a nanocarrier for reaping the nutritional benefits of VitD<sub>3</sub> and SPH.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100399"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142526538","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-01DOI: 10.1016/j.foostr.2024.100396
Md. Hafizur Rahman Bhuiyan, Nushrat Yeasmen, Michael Ngadi
This study investigated the effects of hydrocolloid addition on three-dimensional (3D) printing and cooking of plant ingredients-based meat analog (MA). The MA inks were formulated with soy protein isolate, wheat gluten, canola oil, water, and hydrocolloids (xanthan gum, pectin, hydroxypropyl methylcellulose, guar gum, locust bean gum) at a ratio of 22:12:15:88:2. Formulated inks were used to create a specific 3D cylindrical model geometry and the printed structure were subjected to air frying (AF:180°C, 15 min) and infrared heating (IR:180°C, 15 min). Results showed that the MA ink’s viscosity (3871–5482 Pa. s), 3D printing rate (0.34–0.39 g.sec−1), printing error (2.51–10.37 %), and printing precision (81.97–97.27 %) were significantly (p<0.05) impacted by the incorporation of hydrocolloids. The dimensional stability (63.17–98.58 %), and cooking loss (6.70–17.41 %) were greatly impacted by both the hydrocolloids and post-printing cooking methods. Moisture (1.71 db) and fat (0.28 db) content of uncooked 3D printed MA were identical, whereas, differences in color attributes (L value:80.21–98.88, a value:0.01–0.13, b value:0.11–2.11) among the studied hydrocolloid added samples were observed. Moisture, fat, and color traits of 3D printed meat-analogs were significantly (p<0.05) impacted by post-printing cooking methods (AF, IR). During post-printing cooking, the loss of mass (moisture, fat) and changes in color tones were associated with the types of hydrocolloids incorporated in formulating the 3D printing ink. Surfaces and internal structure, mass loss, chemical profile, and glass-transition-temperature of 3D printed meat-analogs were significantly (p<0.05) impacted by both the type of incorporated hydrocolloids and post-printing cooking methods.
本研究调查了添加亲水胶体对基于植物成分的肉类模拟物（MA）的三维（3D）打印和烹饪的影响。肉类模拟油墨由大豆分离蛋白、小麦面筋、菜籽油、水和水胶体（黄原胶、果胶、羟丙基甲基纤维素、瓜尔豆胶、槐豆胶）按 22:12:15:88:2 的比例配制而成。配制好的油墨用于创建特定几何形状的三维圆柱模型，并对打印结构进行空气油炸（AF:180°C，15 分钟）和红外加热（IR:180°C，15 分钟）。结果表明，加入水胶体后，MA 油墨的粘度（3871-5482 Pa. s）、三维打印速率（0.34-0.39 g.sec-1）、打印误差（2.51-10.37 %）和打印精度（81.97-97.27 %）均受到显著影响（p<0.05）。水胶体和印刷后蒸煮方法对尺寸稳定性（63.17-98.58 %）和蒸煮损失（6.70-17.41 %）都有很大影响。未蒸煮的 3D 打印 MA 的水分（1.71 db）和脂肪（0.28 db）含量相同，而所研究的添加了水胶体的样品在颜色属性（L 值：80.21-98.88，a 值：0.01-0.13，b 值：0.11-2.11）方面存在差异。3D打印肉类样品的水分、脂肪和颜色特征受到打印后烹饪方法（AF、IR）的显著影响（p<0.05）。在打印后烹饪过程中，质量（水分、脂肪）的损失和色调的变化与 3D 打印油墨配方中加入的水胶体类型有关。3D打印肉类样品的表面和内部结构、质量损失、化学特征和玻璃化转变温度均受到所加入的水胶体类型和打印后烹饪方法的显著影响（p<0.05）。
{"title":"Impact of hydrocolloids on 3D meat analog printing and cooking","authors":"Md. Hafizur Rahman Bhuiyan, Nushrat Yeasmen, Michael Ngadi","doi":"10.1016/j.foostr.2024.100396","DOIUrl":"10.1016/j.foostr.2024.100396","url":null,"abstract":"<div><div>This study investigated the effects of hydrocolloid addition on three-dimensional (3D) printing and cooking of plant ingredients-based meat analog (MA). The MA inks were formulated with soy protein isolate, wheat gluten, canola oil, water, and hydrocolloids (xanthan gum, pectin, hydroxypropyl methylcellulose, guar gum, locust bean gum) at a ratio of 22:12:15:88:2. Formulated inks were used to create a specific 3D cylindrical model geometry and the printed structure were subjected to air frying (AF:180°C, 15 min) and infrared heating (IR:180°C, 15 min). Results showed that the MA ink’s viscosity (3871–5482 Pa. s), 3D printing rate (0.34–0.39 g.sec<sup>−1</sup>), printing error (2.51–10.37 %), and printing precision (81.97–97.27 %) were significantly (p<0.05) impacted by the incorporation of hydrocolloids. The dimensional stability (63.17–98.58 %), and cooking loss (6.70–17.41 %) were greatly impacted by both the hydrocolloids and post-printing cooking methods. Moisture (1.71 db) and fat (0.28 db) content of uncooked 3D printed MA were identical, whereas, differences in color attributes (L value:80.21–98.88, a value:0.01–0.13, b value:0.11–2.11) among the studied hydrocolloid added samples were observed. Moisture, fat, and color traits of 3D printed meat-analogs were significantly (p<0.05) impacted by post-printing cooking methods (AF, IR). During post-printing cooking, the loss of mass (moisture, fat) and changes in color tones were associated with the types of hydrocolloids incorporated in formulating the 3D printing ink. Surfaces and internal structure, mass loss, chemical profile, and glass-transition-temperature of 3D printed meat-analogs were significantly (p<0.05) impacted by both the type of incorporated hydrocolloids and post-printing cooking methods.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100396"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142442294","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-10-01DOI: 10.1016/j.foostr.2024.100393
Abbas Jabermoradi , John P.M. van Duynhoven , Johannes Hohlbein
Emulsifiers play an essential role in ensuring the physiochemical stability of food emulsions. In the case of mayonnaise, proteins contained in egg yolk act as emulsifiers. Here, we employed stochastic optical reconstruction microscopy (STORM) to localize proteins at the oil/water droplet interface using fluorescently labeled antibodies. To quantitatively analyze the distribution of proteins, we first simulated homogeneous and heterogeneous distributions. We then implemented the relative position distribution (RPD) analysis to extract the histogram of relative distances between all neighboring localizations. By analyzing the local maxima of the histogram, we could classify distributions at droplet interfaces as homogeneous, partially heterogeneous, and heterogeneous. The model fitting over the RPD histogram using a 2D probability function further provided a localization precision amplitude consistent with the analysis of the local maxima. As a model system for mayonnaise, we used emulsions prepared with combinations of phosvitin, phospholipids, apolipoprotein B (apoB), and sodium dodecyl sulfate (SDS) as emulsifiers. The binary phosvitin/SDS model emulsion showed a partially heterogeneous distribution of phosvitin around the droplets. The ternary phosvitin/phospholipid/SDS and apoB/phospholipid/SDS emulsions showed increased heterogeneity of phosvitin and apoB. Quantification of heterogeneity at droplet interfaces may provide insights in factors determining the physical and chemical stability of emulsions.
{"title":"Quantifying the distribution of proteins at the interface of oil-in-water food emulsions","authors":"Abbas Jabermoradi , John P.M. van Duynhoven , Johannes Hohlbein","doi":"10.1016/j.foostr.2024.100393","DOIUrl":"10.1016/j.foostr.2024.100393","url":null,"abstract":"<div><div>Emulsifiers play an essential role in ensuring the physiochemical stability of food emulsions. In the case of mayonnaise, proteins contained in egg yolk act as emulsifiers. Here, we employed stochastic optical reconstruction microscopy (STORM) to localize proteins at the oil/water droplet interface using fluorescently labeled antibodies. To quantitatively analyze the distribution of proteins, we first simulated homogeneous and heterogeneous distributions. We then implemented the relative position distribution (RPD) analysis to extract the histogram of relative distances between all neighboring localizations. By analyzing the local maxima of the histogram, we could classify distributions at droplet interfaces as homogeneous, partially heterogeneous, and heterogeneous. The model fitting over the RPD histogram using a 2D probability function further provided a localization precision amplitude consistent with the analysis of the local maxima. As a model system for mayonnaise, we used emulsions prepared with combinations of phosvitin, phospholipids, apolipoprotein B (apoB), and sodium dodecyl sulfate (SDS) as emulsifiers. The binary phosvitin/SDS model emulsion showed a partially heterogeneous distribution of phosvitin around the droplets. The ternary phosvitin/phospholipid/SDS and apoB/phospholipid/SDS emulsions showed increased heterogeneity of phosvitin and apoB. Quantification of heterogeneity at droplet interfaces may provide insights in factors determining the physical and chemical stability of emulsions.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100393"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142420496","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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